ID   A0A3Q3XFC8_MOLML        Unreviewed;       877 AA.
AC   A0A3Q3XFC8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMOP00000021546.1};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000021546.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000021546.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC       {ECO:0000256|ARBA:ARBA00009475}.
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DR   AlphaFoldDB; A0A3Q3XFC8; -.
DR   STRING; 94237.ENSMMOP00000021546; -.
DR   Ensembl; ENSMMOT00000021903.1; ENSMMOP00000021546.1; ENSMMOG00000016372.1.
DR   OMA; VKDIGCI; -.
DR   Proteomes; UP000261620; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0051172; P:negative regulation of nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd20599; CYCLIN_RB; 1.
DR   Gene3D; 1.10.472.140; -; 1.
DR   Gene3D; 6.10.140.1380; -; 1.
DR   Gene3D; 6.10.250.530; -; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR002720; RB_A.
DR   InterPro; IPR002719; RB_B.
DR   InterPro; IPR015030; RB_C.
DR   InterPro; IPR028309; RB_fam.
DR   InterPro; IPR024599; RB_N.
DR   PANTHER; PTHR13742:SF17; RETINOBLASTOMA-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR13742; RETINOBLASTOMA-ASSOCIATED PROTEIN RB -RELATED; 1.
DR   Pfam; PF11934; DUF3452; 1.
DR   Pfam; PF01858; RB_A; 1.
DR   Pfam; PF01857; RB_B; 1.
DR   Pfam; PF08934; Rb_C; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SMART; SM01367; DUF3452; 1.
DR   SMART; SM01368; RB_A; 1.
DR   SMART; SM01369; Rb_C; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Cyclin {ECO:0000256|ARBA:ARBA00023127};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          90..199
FT                   /note="Retinoblastoma-associated protein N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01367"
FT   DOMAIN          331..538
FT                   /note="Retinoblastoma-associated protein A-box"
FT                   /evidence="ECO:0000259|SMART:SM01368"
FT   DOMAIN          627..728
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          735..877
FT                   /note="Retinoblastoma-associated protein C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01369"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..596
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..877
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   877 AA;  99866 MW;  2E326908D7E93D0B CRC64;
     MSPKKRNTVA SQNKEQKPSA ESVSPDKENP ELSFKKHRDK DTEFVTLCKS LRVTDLVCEH
     GWTLWKTIQD SMDEVTDTQK RLWGACLFVS VTDMDAACFT LTQLLKAVNL NVKQFLTLVR
     KLDVNLDTIS TKVNSALTRL EKKYDVTLAL YQRFEKQRET IRSCWTMFLL AKGRALQMED
     DLVISFQLLL CTLEFCIKRC TPDLLQPLYG KPQYQPVYHC GSAFRTSYCR SEPPPYLYTF
     LWPFLCVKNV YQTSFSAFLD SLDLLRAPDF PQGNGLNLQY EEHYLKSKDF DGRLFFDGDE
     TVLLPQVEIS QVERTPKKMS DEDNVLIPPQ TPIKAAMTSI QQLRGDLTST GDQPSTNLAT
     YFKNCTVDPT QDVLERLETL GEVFSHRFGQ AVGPHCVALG KQRFNLGVKL YYKVMEAMLK
     SQAHSIFHYS KLLNDSTFHT SLLACALEVV MAAYGESSFK TGGYSHSSGG DAAEKNVCFP
     WILHVVKLAA FDFYKVTESF IKADPTLSKD IVKHLETCEN LIMERIAWMT GSPLFELLKQ
     EHEGGAAEQM ETPASFSQPL QHNHTAADLY LSPIRPGLRV LPPDSPATPC PQASSQPPTQ
     PAGQTPRLPK SNSLSLFYKK LYRLAYTRLK LLCSYLLSSH PELEPIIWTL FQHTLQHEHE
     LMRDRHLDQL MMSAMYAVCK VKSVDLRFKT IVTAYKNMPN TNQETFKHVL ITEDHYDSII
     IFYNQVFMQK LKTNILQYAS TRPPTLSPIP QIPRSPYKFP SSPLRVPGSN NVYISPLKST
     RMSPGIMTPR SRMLVSIGES FGTSDRFQKI NQMVNSSDRS FKRTLDLGSA PKPLKRLRFD
     VDGQDEADGR LIIFHAGSTR SRMQEQKMKE DAESRKE
//